A
Anna Roujeinikova
Researcher at Monash University, Clayton campus
Publications - 78
Citations - 2852
Anna Roujeinikova is an academic researcher from Monash University, Clayton campus. The author has contributed to research in topics: Periplasmic space & Transmembrane domain. The author has an hindex of 22, co-authored 73 publications receiving 2463 citations. Previous affiliations of Anna Roujeinikova include Discovery Institute & University of Leicester.
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Journal ArticleDOI
Molecular basis of triclosan activity
Colin Levy,Anna Roujeinikova,Svetlana E. Sedelnikova,Patrick J. Baker,Antoine R. Stuitje,Antoni R. Slabas,David W. Rice,John B. Rafferty +7 more
TL;DR: It is found that triclosan acts as a site-directed, very potent inhibitor of the enzyme by mimicking its natural substrate.
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Atomic description of an enzyme reaction dominated by proton tunneling
Laura Masgrau,Anna Roujeinikova,Linus O. Johannissen,Parvinder Hothi,Jaswir Basran,Kara E. Ranaghan,Adrian J. Mulholland,Michael J. Sutcliffe,Nigel S. Scrutton,David Leys +9 more
TL;DR: It is shown that, in this enzyme system, tunneling is promoted by a short-range motion modulating proton-acceptor distance and no long-range coupled motion is required.
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Structural Studies of Fatty Acyl-(Acyl Carrier Protein) Thioesters Reveal a Hydrophobic Binding Cavity that Can Expand to Fit Longer Substrates
Anna Roujeinikova,William J. Simon,John Gilroy,David W. Rice,John B. Rafferty,Antoni R. Slabas +5 more
TL;DR: The results not only clarify the means by which a substrate of varying size and complexity is transported in the cell but also suggest a mechanism by which interacting enzymes can recognize the loaded ACP through recognition of surface features including the conformation of the phosphopantetheine linker.
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Crystal structure of the cell wall anchor domain of MotB, a stator component of the bacterial flagellar motor: Implications for peptidoglycan recognition
TL;DR: Significant structural similarities were found between MotB-C and the PG-binding domains of reduction-modifiable protein M and peptidoglycan-associated lipoprotein exclude, suggesting that PG recognition by different outer membrane protein A-like proteins may be governed by very similar molecular mechanisms that evidently involve protein dimerization.
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X-Ray Crystallographic Studies on Butyryl-ACP Reveal Flexibility of the Structure around a Putative Acyl Chain Binding Site
Anna Roujeinikova,Clair Baldock,William J. Simon,John Gilroy,Patrick J. Baker,Antoine R. Stuitje,David W. Rice,Antoni R. Slabas,John B. Rafferty +8 more
TL;DR: The first crystal structures of an acylated form of ACP from E. coli are determined, that of butyryl-ACP, and it is proposed that the protein has adopted the conformation after delivery of substrate into the active site of a partner enzyme.